1wa2
CRYSTAL STRUCTURE OF H313Q MUTANT OF ALCALIGENES XYLOSOXIDANS NITRITE REDUCTASE WITH NITRITE BOUND
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OverviewOverview
Dissimilatory nitrite reductase catalyses the reduction of nitrite to, nitric oxide within the key biological process of denitrification. We, present biochemical and structural results on two key mutants, one, postulated to be important for the interaction with the partner protein, and the other for substrate entry. Trp138, adjacent to one of the type-1, Cu ligands, is one of the residues surrounding a small depression, speculated to be important in complex formation with the physiological, redox partners, azurin I and II. Our data reveal that the Trp138His mutant, is fully active using methyl viologen as an artificial electron donor, but, there is a large decrease in activity using azurin I. These observations, together with its crystal structure at a high resolution of 1.6 A confirm, ... [(full description)]
About this StructureAbout this Structure
1WA2 is a [Single protein] structure of sequence from [Achromobacter xylosoxidans] with CU, ZN, NO2, SO4 and MES as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Insights into redox partner interactions and substrate binding in nitrite reductase from Alcaligenes xylosoxidans: crystal structures of the Trp138His and His313Gln mutants., Barrett ML, Harris RL, Antonyuk S, Hough MA, Ellis MJ, Sawers G, Eady RR, Hasnain SS, Biochemistry. 2004 Dec 28;43(51):16311-9. PMID:15610025
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